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Database: UniProt
Entry: R0KSI0_NOSB1
LinkDB: R0KSI0_NOSB1
Original site: R0KSI0_NOSB1 
ID   R0KSI0_NOSB1            Unreviewed;       339 AA.
AC   R0KSI0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Putative methyltransferase NSUN5 {ECO:0000313|EMBL:EOB13726.1};
GN   Name=NSUN5 {ECO:0000313|EMBL:EOB13726.1};
GN   ORFNames=NBO_62g0016 {ECO:0000313|EMBL:EOB13726.1};
OS   Nosema bombycis (strain CQ1 / CVCC 102059) (Microsporidian parasite)
OS   (Pebrine of silkworm).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578461 {ECO:0000313|EMBL:EOB13726.1, ECO:0000313|Proteomes:UP000016927};
RN   [1] {ECO:0000313|EMBL:EOB13726.1, ECO:0000313|Proteomes:UP000016927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQ1 / CVCC 102059 {ECO:0000313|Proteomes:UP000016927};
RX   PubMed=23496955; DOI=10.1186/1471-2164-14-186;
RA   Pan G., Xu J., Li T., Xia Q., Liu S.L., Zhang G., Li S., Li C., Liu H.,
RA   Yang L., Liu T., Zhang X., Wu Z., Fan W., Dang X., Xiang H., Tao M., Li Y.,
RA   Hu J., Li Z., Lin L., Luo J., Geng L., Wang L., Long M., Wan Y., He N.,
RA   Zhang Z., Lu C., Keeling P.J., Wang J., Xiang Z., Zhou Z.;
RT   "Comparative genomics of parasitic silkworm microsporidia reveal an
RT   association between genome expansion and host adaptation.";
RL   BMC Genomics 14:186-186(2013).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; KB908970; EOB13726.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0KSI0; -.
DR   STRING; 578461.R0KSI0; -.
DR   EnsemblFungi; EOB13726; EOB13726; NBO_62g0016.
DR   VEuPathDB; MicrosporidiaDB:NBO_62g0016; -.
DR   HOGENOM; CLU_005316_7_4_1; -.
DR   OMA; IRSKWHA; -.
DR   Proteomes; UP000016927; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF4; 28S RRNA (CYTOSINE-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000016927};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          77..339
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        297
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         182..188
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         206
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         233
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         251
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   339 AA;  39622 MW;  0DC0CB9D66EFF227 CRC64;
     MKIPKKYREF YTECSLMLKK IIEKKSTIKR EVYKKKNPSE YLAFLDKLVQ NYDLLDKIIT
     AHEFLRKDKF YSVILCYEIL NDKINSQFWK TKFEETKGES EIQHVVKQKF IRLNTLKAKE
     EDLKEMKCDL TSIPNVYKLC SNIDFSTSQL FKDGKIIVQN IASCLPAFLL NPEKDSRVID
     ACSAPGNKTS HLSAIMNNTG KVFAVEVDKY RYNLMKGRLN RFGVKNVKYL NKDFFDIDKD
     EFKNIDYILV DPTCSGSGTH DYYNEDKERT EGLHKFQTKL LKHAMKFGAK KIVYSTCSNN
     KEEGEDVVKA AIAESEYEIY DSSKEYKFLE DLFKFSDLL
//
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